SV2A_PONAB
ID SV2A_PONAB Reviewed; 742 AA.
AC Q5R4L9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Synaptic vesicle glycoprotein 2A;
GN Name=SV2A;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the control of regulated secretion in neural
CC and endocrine cells, enhancing selectively low-frequency
CC neurotransmission. Positively regulates vesicle fusion by maintaining
CC the readily releasable pool of secretory vesicles (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-dependent
CC manner. Binds the adapter protein complex AP-2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Presynapse {ECO:0000250|UniProtKB:Q9JIS5}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules,
CC not present in adrenal microsomes. Associated with both insulin
CC granules and synaptic-like microvesicles in insulin-secreting cells of
CC the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor
CC synaptic terminals. {ECO:0000250|UniProtKB:Q02563,
CC ECO:0000250|UniProtKB:Q9JIS5}.
CC -!- PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain
CC regulates interaction with SYT1. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; CR861227; CAH93297.1; -; mRNA.
DR RefSeq; NP_001126941.1; NM_001133469.1.
DR AlphaFoldDB; Q5R4L9; -.
DR STRING; 9601.ENSPPYP00000001066; -.
DR GeneID; 100173959; -.
DR KEGG; pon:100173959; -.
DR CTD; 9900; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q5R4L9; -.
DR OrthoDB; 724235at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR InterPro; IPR022308; SV2.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR01299; synapt_SV2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..742
FT /note="Synaptic vesicle glycoprotein 2A"
FT /id="PRO_0000239767"
FT TOPO_DOM 1..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..598
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..712
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..742
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Interaction with SYT1"
FT /evidence="ECO:0000250"
FT REGION 40..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS5"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02563"
FT MOD_RES 480
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS5"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 742 AA; 82592 MW; FF2C24AA90CE7078 CRC64;
MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE EEDDDDDFPA
PSDGYYRGEG TQDEEEGGAS SDATEGHDED DEIYEGEYQG IPGAESGGKG ERMADGAPLA
GVRGGLSDGE GPPGGRGEAQ RRKEREELAQ QYEAILRECS HGRFQWTLYF VLGLALMADG
VEVFVVGFVL PSAEKDMCLS DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS
VNSVFAFFSS FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW
MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA LTTQPESPRF
FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI HQEDELIEIQ SDTGTWYQRW
GVRALSLGGQ VWGNFLSCFG PEYRRITLMM MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY
ASRTKVFPGE RVEHVTFNFT LENQIHRGGQ YLNDKFIGLR LKSVSFEDSL FEECYFEDVT
SSNTFFRNCT FINTVFYNTD LFEYKFVNSR LINSTFLHNK EGCPLDVTGT GEGAYMVYFV
SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVMSCVSCF FLSFGNSESA MIALLCLFGG
VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG ISIFTSFVGI TKAAPILFAS
AALALGSSLA LKLPETRGQV LQ
